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Inactivity of μ‐Calpain Throughout Postmortem Aging of Meat
Author(s) -
Kanawa R.,
Ji J.R.,
Takahashi K.
Publication year - 2002
Publication title -
journal of food science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.772
H-Index - 150
eISSN - 1750-3841
pISSN - 0022-1147
DOI - 10.1111/j.1365-2621.2002.tb10651.x
Subject(s) - calpain , myofibril , chemistry , casein , calcium , postmortem changes , sarcoplasm , biochemistry , food science , enzyme , pathology , medicine , organic chemistry
In order to determine the involvement of μ‐calpain in the tenderization of meat during postmortem aging, μ‐calpain was prepared from porcine skeletal muscle and its activity was measured under various conditions, using casein and myofibrils as the substrate. μ‐Calpain was inactive at pH 5.89 and below 15 °C. Even when the reaction time was extended to 10 h, it was entirely inactive at pH 5.62 and 5 °C. In the early postmortem stage, when the pH value of muscle is above 6.0, μ‐calpain was considered to be inactive due to the low concentration of sarcoplasmic calcium ions. μ‐Calpain is, therefore, irrelevant to the tenderization of meat throughout postmortem aging.